Full Chemical Shift Statistics Statistics Calculated for All Chemical Shifts from Atoms in the 20 Common Amino Acids The statistics presented in this table were calculated from the full BMRB database. This includes paramagnetic proteins, proteins with aromatic prosthetic groups, and entries where chemical shifts are reported relative to uncommon chemical shift references. The calculated statistics are drived from a total of 9046374 chemical shifts. Last updated: 8/13/2020 Res Name Atom Count Min. Max. Avg. Std Dev ALA H H 85114 -0.91 69.23 8.19 0.64 ALA HA H 58344 -2.52 17.87 4.24 0.44 ALA HB H 55990 -14.04 5.48 1.35 0.28 ALA C C 54862 0.04 187.20 177.72 3.80 ALA CA C 75384 17.01 354.70 53.17 2.79 ALA CB C 71377 -40.99 318.87 19.06 3.09 ALA N N 81233 0.05 766.00 123.34 6.07 ARG H H 56854 0.01 178.00 8.24 1.06 ARG HA H 39939 1.21 12.57 4.29 0.47 ARG HB2 H 36301 -4.78 27.53 1.79 0.31 ARG HB3 H 34340 -1.32 27.53 1.76 0.32 ARG HG2 H 32438 -1.45 4.20 1.56 0.28 ARG HG3 H 30103 -1.30 5.47 1.54 0.30 ARG HD2 H 31856 -6.44 5.00 3.11 0.27 ARG HD3 H 29018 -0.69 5.00 3.09 0.29 ARG HE H 10789 2.20 116.66 7.45 2.85 ARG HH11 H 966 4.41 11.70 6.94 0.58 ARG HH12 H 737 4.41 10.73 6.88 0.54 ARG HH21 H 825 1.23 11.35 6.82 0.65 ARG HH22 H 677 1.23 60.14 6.91 2.15 ARG C C 34696 0.17 184.96 176.40 3.38 ARG CA C 49092 8.37 358.12 56.78 3.36 ARG CB C 45729 16.52 329.12 30.70 2.52 ARG CG C 27261 12.17 328.29 27.26 3.06 ARG CD C 27502 18.94 342.64 43.20 2.95 ARG CZ C 733 43.20 184.50 160.09 7.41 ARG N N 52730 0.13 433.81 120.81 4.78 ARG NE N 6796 -23.15 149.11 90.10 13.75 ARG NH1 N 277 6.45 124.79 78.51 13.31 ARG NH2 N 239 66.20 128.47 78.61 14.13 ASP H H 67389 -0.35 25.88 8.30 0.59 ASP HA H 46223 -3.75 8.66 4.59 0.33 ASP HB2 H 43153 -5.20 37.40 2.72 0.51 ASP HB3 H 41487 -1.46 37.20 2.67 0.52 ASP HD2 H 18 1.16 12.30 5.99 3.33 ASP C C 42919 0.11 219.00 176.36 3.60 ASP CA C 59428 5.63 354.53 54.69 2.73 ASP CB C 56277 9.70 341.27 40.89 2.57 ASP CG C 962 2.64 188.22 177.87 15.12 ASP N N 64627 0.06 428.09 120.70 4.68 ASN H H 46817 0.01 121.37 8.33 0.98 ASN HA H 32933 0.90 7.11 4.66 0.36 ASN HB2 H 30892 -0.77 8.88 2.80 0.33 ASN HB3 H 29822 -0.95 5.81 2.74 0.36 ASN HD21 H 23247 0.78 111.32 7.34 0.85 ASN HD22 H 22984 0.91 111.32 7.14 0.87 ASN C C 29233 0.11 185.30 175.21 3.59 ASN CA C 41254 2.20 354.02 53.54 3.54 ASN CB C 39143 1.96 342.80 38.73 3.61 ASN CG C 2674 0.00 185.50 176.41 7.15 ASN N N 43945 0.04 426.31 118.94 5.14 ASN ND2 N 20143 21.04 1114.29 112.91 12.69 CYS H H 23438 3.72 12.66 8.38 0.70 CYS HA H 19202 -9.86 43.50 4.68 0.98 CYS HB2 H 18504 -39.82 363.58 3.14 6.39 CYS HB3 H 18034 -44.20 363.58 3.06 5.79 CYS HG H 249 -1.83 10.70 2.00 1.34 CYS C C 11198 1.00 187.59 174.77 3.49 CYS CA C 16849 30.67 82.30 58.00 3.45 CYS CB C 16081 17.99 73.92 33.40 6.52 CYS N N 18559 -147.00 628.00 120.45 18.37 GLU H H 87401 0.01 122.90 8.33 0.75 GLU HA H 60339 0.43 8.76 4.24 0.41 GLU HB2 H 54641 -1.47 4.82 2.02 0.22 GLU HB3 H 51427 -1.63 8.10 1.99 0.23 GLU HG2 H 50438 -0.67 4.69 2.26 0.22 GLU HG3 H 47012 -0.10 4.69 2.24 0.22 GLU HE2 H 18 0.80 11.96 4.71 2.60 GLU C C 56628 0.07 190.58 176.82 4.31 GLU CA C 77301 1.06 360.83 57.33 3.29 GLU CB C 72242 9.08 330.83 30.02 3.17 GLU CG C 45202 6.16 337.23 36.14 2.96 GLU CD C 1012 7.02 198.61 181.25 13.71 GLU N N 84087 0.04 422.04 120.71 4.72 GLN H H 47736 0.00 66.54 8.22 0.65 GLN HA H 33047 0.40 7.43 4.26 0.43 GLN HB2 H 30091 -1.51 10.46 2.04 0.28 GLN HB3 H 28651 -1.50 20.90 2.01 0.33 GLN HG2 H 28095 -1.76 33.60 2.31 0.34 GLN HG3 H 26079 -1.40 34.95 2.29 0.36 GLN HE21 H 21203 -3.41 23.89 7.22 0.50 GLN HE22 H 21086 1.03 113.70 7.04 0.88 GLN C C 30550 0.07 1756.00 176.33 9.73 GLN CA C 42543 1.73 356.83 56.56 2.65 GLN CB C 39872 1.84 328.29 29.20 2.54 GLN CG C 24913 2.10 333.03 33.80 2.57 GLN CD C 2585 6.79 190.62 179.35 7.06 GLN N N 45708 0.00 418.06 119.95 4.19 GLN NE2 N 19101 33.90 412.16 111.88 3.00 GLY H H 84495 -15.30 121.88 8.33 0.77 GLY HA2 H 57431 -3.40 8.64 3.96 0.40 GLY HA3 H 54761 -3.94 7.69 3.89 0.41 GLY C C 53419 1.00 189.53 173.84 3.45 GLY CA C 74948 2.20 344.99 45.38 2.23 GLY N N 79522 0.20 791.00 109.68 7.11 HIS H H 24023 -0.30 13.34 8.26 0.73 HIS HA H 17427 0.68 11.38 4.62 0.57 HIS HB2 H 16281 -2.17 45.90 3.16 1.12 HIS HB3 H 15829 -6.20 38.50 3.10 1.09 HIS HD1 H 1019 -15.00 86.50 10.00 8.57 HIS HD2 H 11477 -25.85 67.80 7.16 3.30 HIS HE1 H 9022 -26.60 134.81 7.83 2.58 HIS HE2 H 392 -15.00 76.40 11.10 7.86 HIS C C 14862 1.00 184.20 175.12 4.74 HIS CA C 21529 11.40 355.08 56.51 3.42 HIS CB C 20224 13.50 329.05 30.33 3.19 HIS CG C 260 60.97 139.83 131.52 6.67 HIS CD2 C 7411 7.19 159.95 119.91 5.73 HIS CE1 C 5806 8.20 166.28 137.23 5.76 HIS N N 22448 0.20 427.15 119.66 5.23 HIS ND1 N 805 31.03 261.01 193.20 32.73 HIS NE2 N 744 17.00 257.57 180.90 20.56 ILE H H 58716 0.01 11.87 8.26 0.69 ILE HA H 40736 -9.00 173.54 4.17 1.01 ILE HB H 38348 -2.44 38.70 1.78 0.40 ILE HG12 H 34816 -10.10 5.56 1.26 0.45 ILE HG13 H 33489 -10.10 9.71 1.19 0.49 ILE HG2 H 36729 -3.92 6.23 0.77 0.31 ILE HD1 H 38359 -4.15 13.89 0.67 0.34 ILE C C 37603 0.00 187.55 175.79 4.56 ILE CA C 52130 20.88 362.18 61.62 3.37 ILE CB C 48634 -34.48 339.79 38.59 2.94 ILE CG1 C 30937 8.00 329.29 27.75 3.36 ILE CG2 C 32814 0.79 317.62 17.61 3.26 ILE CD1 C 34368 2.70 314.60 13.51 3.50 ILE N N 56106 0.00 531.00 121.43 6.08 LEU H H 97230 -0.30 13.22 8.22 0.65 LEU HA H 67061 0.00 119.41 4.30 0.65 LEU HB2 H 61683 -1.52 8.02 1.61 0.36 LEU HB3 H 59179 -1.79 8.39 1.52 0.38 LEU HG H 54602 -2.08 5.70 1.50 0.35 LEU HD1 H 62298 -3.42 30.18 0.75 0.33 LEU HD2 H 59963 -3.42 24.50 0.73 0.36 LEU C C 62323 0.07 228.49 176.98 3.71 LEU CA C 86222 1.06 158.32 55.65 2.24 LEU CB C 80611 7.44 93.18 42.25 2.02 LEU CG C 47749 0.00 75.28 26.80 1.50 LEU CD1 C 53939 0.68 120.70 24.67 2.05 LEU CD2 C 51574 0.28 116.30 24.11 2.13 LEU N N 92600 0.04 627.00 121.96 7.82 LYS H H 82398 0.00 64.42 8.18 0.67 LYS HA H 58028 -0.12 32.65 4.26 0.46 LYS HB2 H 52268 -1.42 10.94 1.77 0.27 LYS HB3 H 49254 -3.04 9.43 1.75 0.28 LYS HG2 H 47273 -1.65 6.70 1.36 0.27 LYS HG3 H 43570 -1.83 5.58 1.35 0.28 LYS HD2 H 41986 -1.68 119.62 1.61 0.65 LYS HD3 H 37630 -2.02 29.05 1.59 0.27 LYS HE2 H 41249 -0.49 42.02 2.91 0.29 LYS HE3 H 36319 -0.05 7.34 2.90 0.22 LYS HZ H 1605 -10.90 10.51 7.33 1.05 LYS C C 50607 0.11 996.25 176.61 5.78 LYS CA C 70569 1.16 359.22 56.94 3.22 LYS CB C 65882 -26.69 332.99 32.80 2.94 LYS CG C 40529 12.11 325.49 24.96 3.15 LYS CD C 38172 0.83 329.28 29.00 2.65 LYS CE C 36836 -0.13 342.33 41.93 3.06 LYS N N 76851 0.04 427.25 121.04 4.72 LYS NZ N 300 1.95 177.20 50.86 32.23 MET H H 22917 -0.21 177.00 8.26 1.27 MET HA H 16483 -0.93 313.57 4.41 2.46 MET HB2 H 14773 -27.31 33.75 2.02 0.59 MET HB3 H 13936 -27.31 12.94 1.99 0.52 MET HG2 H 13554 -33.86 32.70 2.36 1.59 MET HG3 H 12830 -33.86 31.70 2.34 1.70 MET HE H 10329 -24.86 10.20 1.75 1.71 MET C C 15121 2.20 183.25 176.18 3.35 MET CA C 21385 25.73 85.33 56.14 2.29 MET CB C 19765 0.20 332.17 32.99 3.24 MET CG C 11647 2.30 332.69 32.08 3.26 MET CE C 9314 0.00 317.65 17.26 4.31 MET N N 22131 0.00 428.25 120.06 5.04 PHE H H 41905 -0.50 12.18 8.34 0.73 PHE HA H 28749 1.33 59.70 4.62 0.73 PHE HB2 H 26840 -0.46 7.98 2.99 0.38 PHE HB3 H 26178 -0.21 12.72 2.93 0.40 PHE HD1 H 22344 0.60 12.15 7.04 0.40 PHE HD2 H 19034 0.60 12.15 7.04 0.41 PHE HE1 H 19489 -2.84 14.08 7.06 0.46 PHE HE2 H 16816 0.00 12.90 7.06 0.45 PHE HZ H 13779 -7.14 43.62 6.99 0.72 PHE C C 26274 0.09 187.61 175.45 3.09 PHE CA C 36651 4.92 363.62 58.10 3.84 PHE CB C 34382 2.16 341.70 39.96 3.63 PHE CG C 409 7.23 152.84 137.51 10.33 PHE CD1 C 13286 7.16 143.45 131.16 6.01 PHE CD2 C 9586 7.16 140.31 131.33 4.47 PHE CE1 C 11547 0.00 149.61 130.31 5.86 PHE CE2 C 8321 7.47 149.61 130.54 3.92 PHE CZ C 8750 7.35 165.61 129.01 4.20 PHE N N 39670 0.07 422.84 120.39 5.48 PRO H2 H 5 8.07 9.67 8.76 0.71 PRO HA H 32919 0.64 135.80 4.39 0.81 PRO HB2 H 30611 -1.50 5.63 2.07 0.37 PRO HB3 H 29720 -3.48 6.10 1.99 0.38 PRO HG2 H 27505 -2.35 7.40 1.92 0.34 PRO HG3 H 25586 -1.52 4.92 1.89 0.35 PRO HD2 H 28298 -6.56 7.67 3.64 0.45 PRO HD3 H 27321 -6.56 8.87 3.60 0.47 PRO C C 28194 0.00 183.52 176.63 4.42 PRO CA C 40448 0.00 363.09 63.33 3.63 PRO CB C 37761 0.00 333.59 31.89 3.18 PRO CG C 24721 2.44 327.40 27.28 3.74 PRO CD C 24826 1.16 350.65 50.34 3.22 PRO N N 1958 3.57 430.00 135.18 25.10 SER H H 70861 -15.30 116.96 8.28 0.73 SER HA H 50110 1.28 58.74 4.48 0.48 SER HB2 H 45926 0.61 9.18 3.87 0.28 SER HB3 H 42654 0.61 41.70 3.84 0.34 SER HG H 907 0.13 11.36 5.43 1.20 SER C C 45761 0.00 197.10 174.59 3.28 SER CA C 64437 4.33 361.28 58.69 2.81 SER CB C 59810 -939.28 365.09 63.72 5.01 SER N N 67149 0.00 416.96 116.29 4.27 THR H H 63300 0.02 21.70 8.23 0.64 THR HA H 43969 -1.50 7.47 4.45 0.48 THR HB H 40381 0.09 71.59 4.17 0.66 THR HG1 H 1605 -1.78 11.01 5.21 1.41 THR HG2 H 40119 -12.10 16.30 1.14 0.28 THR C C 39732 4.78 185.92 174.45 4.10 THR CA C 55725 0.97 92.66 62.21 2.76 THR CB C 51742 -939.28 629.21 69.60 5.68 THR CG2 C 33901 7.18 175.60 21.60 1.93 THR N N 60215 0.00 402.00 115.40 6.35 TRP H H 13952 3.42 17.32 8.27 0.78 TRP HA H 9734 2.04 11.41 4.68 0.54 TRP HB2 H 9225 0.42 5.35 3.18 0.35 TRP HB3 H 8966 -0.38 7.97 3.12 0.37 TRP HD1 H 8207 1.88 10.75 7.13 0.37 TRP HE1 H 9133 -1.28 131.71 10.09 1.45 TRP HE3 H 7114 1.85 12.23 7.30 0.53 TRP HZ2 H 7711 2.63 10.81 7.27 0.41 TRP HZ3 H 6858 0.76 8.90 6.85 0.47 TRP HH2 H 7078 2.84 10.90 6.95 0.46 TRP C C 8374 2.50 184.30 175.97 6.08 TRP CA C 11774 2.97 362.10 57.71 4.82 TRP CB C 10982 1.60 328.80 30.10 4.79 TRP CG C 252 4.17 116.53 110.08 9.13 TRP CD1 C 5208 30.24 183.14 126.31 4.49 TRP CD2 C 182 1.58 155.17 127.03 13.27 TRP CE2 C 239 56.42 177.71 137.57 9.67 TRP CE3 C 4347 -10.87 174.81 120.16 5.58 TRP CZ2 C 4982 7.11 159.04 114.04 4.63 TRP CZ3 C 4373 -8.70 161.54 121.15 4.69 TRP CH2 C 4615 -6.33 160.82 123.54 5.04 TRP N N 12729 6.71 423.16 121.65 6.06 TRP NE1 N 7477 0.53 435.96 129.26 6.33 TYR H H 35875 0.02 12.34 8.30 0.74 TYR HA H 24789 0.44 7.16 4.61 0.56 TYR HB2 H 23129 -21.23 23.28 2.90 0.47 TYR HB3 H 22610 -21.23 23.28 2.83 0.48 TYR HD1 H 19874 0.19 10.50 6.92 0.37 TYR HD2 H 17062 0.55 10.50 6.91 0.38 TYR HE1 H 18838 0.08 11.80 6.69 0.31 TYR HE2 H 16280 0.43 11.70 6.69 0.32 TYR HH H 434 -0.79 31.00 9.11 2.10 TYR C C 21887 2.20 184.78 175.35 4.73 TYR CA C 30620 2.20 357.68 58.13 3.11 TYR CB C 28455 18.38 338.69 39.32 3.14 TYR CG C 380 7.11 144.30 128.54 9.73 TYR CD1 C 12065 19.59 141.57 132.37 5.22 TYR CD2 C 8396 3.49 139.64 132.38 5.16 TYR CE1 C 11870 40.44 182.76 117.73 4.13 TYR CE2 C 8259 34.12 154.10 117.77 3.36 TYR CZ C 280 6.84 165.72 155.47 13.89 TYR N N 33412 0.20 818.00 120.76 12.00 VAL H H 77191 -0.41 120.98 8.27 0.79 VAL HA H 53482 -2.83 54.97 4.17 0.63 VAL HB H 49946 -27.48 31.75 1.98 0.45 VAL HG1 H 50122 -27.20 24.20 0.82 0.33 VAL HG2 H 49189 -27.20 56.56 0.80 0.43 VAL C C 49833 1.00 205.70 175.63 3.43 VAL CA C 68629 20.67 362.06 62.50 3.20 VAL CB C 63674 15.60 331.75 32.72 2.29 VAL CG1 C 43952 -7.40 321.19 21.55 2.45 VAL CG2 C 42413 -5.65 320.42 21.34 2.54 VAL N N 74211 0.20 529.00 121.14 7.41